1ajh

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(New page: 200px<br /><applet load="1ajh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ajh, resolution 1.69&Aring;" /> '''PHOTOPRODUCT OF CARB...)
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[[Image:1ajh.gif|left|200px]]<br /><applet load="1ajh" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ajh, resolution 1.69&Aring;" />
caption="1ajh, resolution 1.69&Aring;" />
'''PHOTOPRODUCT OF CARBONMONOXY MYOGLOBIN AT 40 K'''<br />
'''PHOTOPRODUCT OF CARBONMONOXY MYOGLOBIN AT 40 K'''<br />
==Overview==
==Overview==
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Myoglobin's reversible binding of oxygen is a model for studies of protein, control of ligand binding and discrimination. Protein relaxation and, geminate ligand rebinding subsequent to ligand photodissociation have been, studied extensively by a variety of techniques. The ps to ns time scales, for these processes are still much shorter than the ms time resolution of, X-ray diffraction experiments, but it may be possible to trap these, intermediates at low temperatures. We report here an X-ray diffraction, investigation of structural changes induced by photolysis of carbonmonoxy, myoglobin crystals at 40 K. Our results provide a structural basis for the, interpretation of ambient and low temperature spectroscopic observations, and molecular dynamics simulations of the ligand photodissociation and, binding processes in haem proteins.
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Myoglobin's reversible binding of oxygen is a model for studies of protein control of ligand binding and discrimination. Protein relaxation and geminate ligand rebinding subsequent to ligand photodissociation have been studied extensively by a variety of techniques. The ps to ns time scales for these processes are still much shorter than the ms time resolution of X-ray diffraction experiments, but it may be possible to trap these intermediates at low temperatures. We report here an X-ray diffraction investigation of structural changes induced by photolysis of carbonmonoxy myoglobin crystals at 40 K. Our results provide a structural basis for the interpretation of ambient and low temperature spectroscopic observations and molecular dynamics simulations of the ligand photodissociation and binding processes in haem proteins.
==About this Structure==
==About this Structure==
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1AJH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon] with SO4, HEM and CMO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AJH OCA].
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1AJH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=CMO:'>CMO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AJH OCA].
==Reference==
==Reference==
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[[Category: Moffat, K.]]
[[Category: Moffat, K.]]
[[Category: Srajer, V.]]
[[Category: Srajer, V.]]
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[[Category: Teng, T.Y.]]
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[[Category: Teng, T Y.]]
[[Category: CMO]]
[[Category: CMO]]
[[Category: HEM]]
[[Category: HEM]]
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[[Category: respiratory protein]]
[[Category: respiratory protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:54:24 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:45:11 2008''

Revision as of 09:45, 21 February 2008


1ajh, resolution 1.69Å

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PHOTOPRODUCT OF CARBONMONOXY MYOGLOBIN AT 40 K

Overview

Myoglobin's reversible binding of oxygen is a model for studies of protein control of ligand binding and discrimination. Protein relaxation and geminate ligand rebinding subsequent to ligand photodissociation have been studied extensively by a variety of techniques. The ps to ns time scales for these processes are still much shorter than the ms time resolution of X-ray diffraction experiments, but it may be possible to trap these intermediates at low temperatures. We report here an X-ray diffraction investigation of structural changes induced by photolysis of carbonmonoxy myoglobin crystals at 40 K. Our results provide a structural basis for the interpretation of ambient and low temperature spectroscopic observations and molecular dynamics simulations of the ligand photodissociation and binding processes in haem proteins.

About this Structure

1AJH is a Single protein structure of sequence from Physeter catodon with , and as ligands. Full crystallographic information is available from OCA.

Reference

Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K., Teng TY, Srajer V, Moffat K, Nat Struct Biol. 1994 Oct;1(10):701-5. PMID:7634074

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